GCSH_BOVIN
ID GCSH_BOVIN Reviewed; 173 AA.
AC P20821; Q0P5G3;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial {ECO:0000303|PubMed:2211640};
DE AltName: Full=Lipoic acid-containing protein;
DE Flags: Precursor;
GN Name=GCSH {ECO:0000250|UniProtKB:P23434};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-78 AND 97-115,
RP LIPOYLATION AT LYS-107, COFACTOR, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=2211640; DOI=10.1016/s0021-9258(18)38186-9;
RA Fujiwara K., Okamura-Ikeda K., Motokawa Y.;
RT "cDNA sequence, in vitro synthesis, and intramitochondrial lipoylation of
RT H-protein of the glycine cleavage system.";
RL J. Biol. Chem. 265:17463-17467(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 49-65, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=3080335; DOI=10.1016/0014-5793(86)80136-3;
RA Waki N., Hiwatashi A., Ichikawa Y.;
RT "Purification and biochemical characterization of hepatic ferredoxin
RT (hepatoredoxin) from bovine liver mitochondria.";
RL FEBS Lett. 195:87-91(1986).
RN [4]
RP PROTEIN SEQUENCE OF 49-63, AND SUBCELLULAR LOCATION.
RX PubMed=2553401; DOI=10.1111/j.1432-1033.1989.tb15100.x;
RA Driscoll W.J., Omdahl J.L.;
RT "Characterization and N-terminal amino acid sequence of multiple
RT ferredoxins in kidney and adrenal mitochondria.";
RL Eur. J. Biochem. 185:181-187(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (0.88 ANGSTROMS) OF 49-173.
RX PubMed=20516622; DOI=10.1107/s0907444910010668;
RA Higashiura A., Kurakane T., Matsuda M., Suzuki M., Inaka K., Sato M.,
RA Kobayashi T., Tanaka T., Tanaka H., Fujiwara K., Nakagawa A.;
RT "High-resolution X-ray crystal structure of bovine H-protein at 0.88 A
RT resolution.";
RL Acta Crystallogr. D 66:698-708(2010).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The H protein (GCSH) shuttles the methylamine group of glycine
CC from the P protein (GLDC) to the T protein (GCST).
CC {ECO:0000250|UniProtKB:P11183}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000269|PubMed:2211640};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000269|PubMed:2211640};
CC -!- SUBUNIT: Interacts with GLDC (By similarity). The glycine cleavage
CC system is composed of four proteins: P (GLDC), T (GCST), L (DLD) and H
CC (GCSH). {ECO:0000250|UniProtKB:P11183}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:2211640,
CC ECO:0000269|PubMed:2553401, ECO:0000269|PubMed:3080335}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:3080335 and PubMed:2553401) thought to
CC be a ferredoxin. {ECO:0000305}.
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DR EMBL; M58361; AAA62710.1; -; mRNA.
DR EMBL; BC120070; AAI20071.1; -; mRNA.
DR PIR; A39214; GCBOH.
DR RefSeq; NP_777269.1; NM_174844.1.
DR RefSeq; XP_005218441.1; XM_005218384.2.
DR PDB; 3KLR; X-ray; 0.88 A; A=49-173.
DR PDB; 3WDN; X-ray; 0.86 A; A=49-173.
DR PDBsum; 3KLR; -.
DR PDBsum; 3WDN; -.
DR AlphaFoldDB; P20821; -.
DR SMR; P20821; -.
DR STRING; 9913.ENSBTAP00000008936; -.
DR PaxDb; P20821; -.
DR PeptideAtlas; P20821; -.
DR PRIDE; P20821; -.
DR Ensembl; ENSBTAT00000008936; ENSBTAP00000008936; ENSBTAG00000006795.
DR GeneID; 317723; -.
DR KEGG; bta:317723; -.
DR CTD; 2653; -.
DR VEuPathDB; HostDB:ENSBTAG00000006795; -.
DR eggNOG; KOG3373; Eukaryota.
DR GeneTree; ENSGT00390000011666; -.
DR HOGENOM; CLU_097408_1_1_1; -.
DR InParanoid; P20821; -.
DR OMA; FARQAWA; -.
DR OrthoDB; 1348095at2759; -.
DR TreeFam; TF300258; -.
DR BRENDA; 1.4.1.27; 908.
DR Reactome; R-BTA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-BTA-6783984; Glycine degradation.
DR EvolutionaryTrace; P20821; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000006795; Expressed in caput epididymis and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
DR CDD; cd06848; GCS_H; 1.
DR HAMAP; MF_00272; GcvH; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR002930; GCV_H.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR017453; GCV_H_sub.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR11715; PTHR11715; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR00527; gcvH; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lipoyl; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2211640,
FT ECO:0000269|PubMed:2553401, ECO:0000269|PubMed:3080335"
FT CHAIN 49..173
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /id="PRO_0000010722"
FT DOMAIN 66..148
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 107
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:2211640"
FT CONFLICT 49
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3WDN"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3WDN"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:3WDN"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3WDN"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:3WDN"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3WDN"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:3WDN"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3WDN"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3WDN"
FT TURN 138..142
FT /evidence="ECO:0007829|PDB:3WDN"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:3WDN"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:3WDN"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3WDN"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:3WDN"
SQ SEQUENCE 173 AA; 18791 MW; 6FBF64293B465D22 CRC64;
MALRAVRSVR AAVGGLRAIS APSAPCLPRP WGLRAGAVRE LRTGPALLSV RKFTEKHEWV
TTENGVGTVG ISNFAQEALG DVVYCSLPEV GTKLNKQEEF GALESVKAAS ELYSPLSGEV
TEINKALAEN PGLVNKSCYE DGWLIKMTFS NPSELDELMS EEAYEKYIKS IEE
